Characterization of an extreme alkaline-stable keratinase from the draft genome of feather-degrading <i>Bacillus</i> sp. JM7 from deep-sea

Jin Min; Chen Chen; He Xiongfei; Zeng Runying

doi:10.1007/s13131-019-1350-5

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Article Navigation > Acta Oceanologica Sinica > 2019 > 38(2): 87-95

Jin Min, Chen Chen, He Xiongfei, Zeng Runying. Characterization of an extreme alkaline-stable keratinase from the draft genome of feather-degrading Bacillus sp. JM7 from deep-sea[J]. Acta Oceanologica Sinica, 2019, 38(2): 87-95. doi: 10.1007/s13131-019-1350-5

Citation:

Jin Min, Chen Chen, He Xiongfei, Zeng Runying. Characterization of an extreme alkaline-stable keratinase from the draft genome of feather-degrading Bacillus sp. JM7 from deep-sea[J]. Acta Oceanologica Sinica, 2019, 38(2): 87-95. doi: 10.1007/s13131-019-1350-5

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Characterization of an extreme alkaline-stable keratinase from the draft genome of feather-degrading Bacillus sp. JM7 from deep-sea

doi: 10.1007/s13131-019-1350-5

1.
State Key Laboratory Breeding Base of Marine Genetic Resource;Third Institute of Oceanography, Ministry of Natural Resources, Xiamen 361005, China
2.
State Key Laboratory Breeding Base of Marine Genetic Resource;Third Institute of Oceanography, Ministry of Natural Resources, Xiamen 361005, China;South China Sea Bio-Resource Exploitation and Utilization Collaborative Innovation Center, Guangzhou 510000, China;Fujian Collaborative Innovation Center for Exploitation and Utilization of Marine Biological Resources, Xiamen 361005, China

Received Date: 2017-05-04

Abstract

Abstract

Bacillus sp. JM7, a strain isolated from the deep-sea of the South China Sea, was found to efficiently degrade 79.4% native chicken feather within 30 h. Scanning electron microscopy analysis showed that JM7 strain could gradually degrade feather by modifying the microstructure of feather keratin. A total of 25 protease genes were predicted from the draft genome of JM7 strain, among which a predicted subtilisin-like serine protease (designated as Ker02562) was further characterized for its keratinolytic activity. The recombinant Ker02562 functioned at a wide range of temperatures from 30℃ to 60℃, with an optimum at 40-50℃. Ker02562 was highly active at various pHs ranging from 5.0 to 13.0, with a maximum activity observed at pH 7.0-9.0. Remarkably, recombinant Ker02562 was stable in extreme alkaline environments (pH 10-13), which was much better than most other reported keratinases. Collectively, these favorable properties could make Bacillus sp. JM7 and Ker02562 attractive to be applied in the detergent formulation and feather bioconversion.
- Bacillus,
- deep-sea,
- feather-degradation,
- keratinases,
- feather bioconversion,
- alkaline-stable

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References(34)

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